Reversible Conversion of Disulfide/Dithiolate Occurring at a Vanadium(IV) Center: A Biomimetic System for Redox...

Ascidians use a class of cysteine-rich proteins generally referred to as vanabins to reduce vanadium ions, one of the many biological processes that involve the redox conversion between disulfide and dithiolate mediated by transition-metal ions. To further understand the nature of disulfide/dithiolate exchange facilitated by a vanadium center, we report herein a six-coordinate non-oxido V^IV complex containing an unbound disulfide moiety, [V^IV(PS3″)(PS1″^S-S)] (1) (PS3″ = [P(C₆H₃-3-Me₃Si-2-S)₃]^3-, where PS1″^S-S is a disulfide form of PS3″). Complex 1 is obtained from a reaction of previously reported [V^V(PS3″)(PS2″S^H)] (2) (PS2″S^H = [P(C₆H₃-3-Me₃Si-2-SH)(C₆H₃-3-Me₃Si-2-S)₂] with TEMPO (TEMPO = 2,2,6,6-tetramethylpiperidin-1-yl)oxyl) via hydrogen atom transfer. Importantly, complex 1 can be reduced by two electrons to form an eight-coordinate V^IV complex, [V^IV(PS3″)₂]^2- (4). The reaction can be reversed through a two-electron oxidation process to regenerate complex 1. The redox pathways both proceed through a common intermediate, [V(PS3″)₂]^- (3), that has been previously reported as a resonance form of V^V-dithiolate and a V^IV-(thiolate)(thiyl-radical) species. This work demonstrates an unprecedented example of reversible disulfide/dithiolate interconversion mediated by a V^IV center, as well as provides insights into understanding the function of V^V reductases in vanabins.